Abstract
AbstractThe lipase‐catalyzed esterification of sorbitan with oleic acid in a solvent‐free system to form sorbitan oleate (commercial name Span80) was studied as a feasible approach aimed at meeting the demand for sugar alcohol‐based surfactants. Screened results obtained from enzymatic synthesis of sorbitan oleate indicated that Novozym 435 had its highest catalytic activity in a solvent‐free system. The introduction of a reduced‐pressure system increased the production of sorbitan oleate to a maximum of 95% of theoretical, obtained from 0.2 mol sorbitan, 0.1 mol oleic acid, and 2.0 g lipase (6 wt% of sorbitan) in a solvent‐free reaction mixture at optimal reaction conditions. Results obtained from lipase‐catalyzed batch esterification reactions showed that more than 90% conversion of sorbitan oleate was maintained after 10 batches of esterification reactions, indicating excellent enzyme stability. Subsequent analysis by HPLC indicated that the product of enzyme‐catalyzed esterification by the immobilized lipase contained a significantly greater amount of monoester (about 80%) compared to the composition obtained by chemical synthesis (about 50%).
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